CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012168
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cullin-1 
Protein Synonyms/Alias
 CUL-1 
Gene Name
 CUL1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
131EDYRFSSKVLNGICAubiquitination[1, 2, 3, 4]
290TQDELARKCEQVLIEubiquitination[5]
410INNNAVTKMAQSSSKubiquitination[1, 3, 4, 5, 6, 7, 8, 9]
417KMAQSSSKSPELLARubiquitination[5]
431RYCDSLLKKSSKNPEacetylation[4]
432YCDSLLKKSSKNPEEubiquitination[5]
464EDKDVFQKFYAKMLAubiquitination[1, 3]
468VFQKFYAKMLAKRLVubiquitination[1, 3, 5]
493ASMISKLKQACGFEYubiquitination[5]
522KDLNEQFKKHLTNSEubiquitination[5]
689VNINVPMKTEQKQEQubiquitination[4, 6]
693VPMKTEQKQEQETTHubiquitination[6]
708KNIEEDRKLLIQAAIubiquitination[3, 10]
720AAIVRIMKMRKVLKHubiquitination[10]
751PRVPVIKKCIDILIEubiquitination[5]
769LERVDGEKDTYSYLAubiquitination[4, 5, 6, 8, 9]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [7] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [8] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [9] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [10] Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry.
 Denis NJ, Vasilescu J, Lambert JP, Smith JC, Figeys D.
 Proteomics. 2007 Mar;7(6):868-74. [PMID: 17370265] 
Functional Description
 Core component of multiple cullin-RING-based SCF (SKP1- CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. May contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and exchange of the substrate recognition component is mediated by TIP120A/CAND1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9) direct ubiquitination of TTI1 and TELO2. 
Sequence Annotation
 CROSSLNK 708 708 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 720 720 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Complete proteome; Host-virus interaction; Isopeptide bond; Reference proteome; Ubl conjugation; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 776 AA 
Protein Sequence
MSSTRSQNPH GLKQIGLDQI WDDLRAGIQQ VYTRQSMAKS RYMELYTHVY NYCTSVHQSN 60
QARGAGVPPS KSKKGQTPGG AQFVGLELYK RLKEFLKNYL TNLLKDGEDL MDESVLKFYT 120
QQWEDYRFSS KVLNGICAYL NRHWVRRECD EGRKGIYEIY SLALVTWRDC LFRPLNKQVT 180
NAVLKLIEKE RNGETINTRL ISGVVQSYVE LGLNEDDAFA KGPTLTVYKE SFESQFLADT 240
ERFYTRESTE FLQQNPVTEY MKKAEARLLE EQRRVQVYLH ESTQDELARK CEQVLIEKHL 300
EIFHTEFQNL LDADKNEDLG RMYNLVSRIQ DGLGELKKLL ETHIHNQGLA AIEKCGEAAL 360
NDPKMYVQTV LDVHKKYNAL VMSAFNNDAG FVAALDKACG RFINNNAVTK MAQSSSKSPE 420
LLARYCDSLL KKSSKNPEEA ELEDTLNQVM VVFKYIEDKD VFQKFYAKML AKRLVHQNSA 480
SDDAEASMIS KLKQACGFEY TSKLQRMFQD IGVSKDLNEQ FKKHLTNSEP LDLDFSIQVL 540
SSGSWPFQQS CTFALPSELE RSYQRFTAFY ASRHSGRKLT WLYQLSKGEL VTNCFKNRYT 600
LQASTFQMAI LLQYNTEDAY TVQQLTDSTQ IKMDILAQVL QILLKSKLLV LEDENANVDE 660
VELKPDTLIK LYLGYKNKKL RVNINVPMKT EQKQEQETTH KNIEEDRKLL IQAAIVRIMK 720
MRKVLKHQQL LGEVLTQLSS RFKPRVPVIK KCIDILIEKE YLERVDGEKD TYSYLA 776 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
 GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
 GO:0007050; P:cell cycle arrest; TAS:ProtInc.
 GO:0008283; P:cell proliferation; IEA:Compara.
 GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
 GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:ProtInc.
 GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
 GO:0007219; P:Notch signaling pathway; TAS:Reactome.
 GO:0009887; P:organ morphogenesis; IEA:Compara.
 GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
 GO:0006513; P:protein monoubiquitination; IEA:Compara.
 GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
 GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR016157; Cullin_CS.
 IPR016158; Cullin_homology.
 IPR001373; Cullin_N.
 IPR019559; Cullin_neddylation_domain.
 IPR016159; Cullin_repeat-like_dom.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF00888; Cullin
 PF10557; Cullin_Nedd8 
SMART
 SM00182; CULLIN
 SM00884; Cullin_Nedd8 
PROSITE
 PS01256; CULLIN_1
 PS50069; CULLIN_2 
PRINTS